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Volumn 1821, Issue 11, 2012, Pages 1425-1433

Rat and human fatty acid amide hydrolases: Overt similarities and hidden differences

Author keywords

Anandamide hydrolase; Endocannabinoid; Fluorescence; Membrane binding; Protein aggregation and stability

Indexed keywords

ANANDAMIDE; ARACHIDONIC ACID DERIVATIVE; FATTY ACID AMIDASE; MEMBRANE PROTEIN; METHOXYARACHIDONYL FLUOROPHOSPHONATE; OLEAMIDE; PHOSPHONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84865302914     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2012.07.021     Document Type: Article
Times cited : (18)

References (65)
  • 1
    • 77950644306 scopus 로고    scopus 로고
    • CB(1) cannabinoid receptors and their associated proteins
    • A.C. Howlett, L.C. Blume, and G.D. Dalton CB(1) cannabinoid receptors and their associated proteins Curr. Med. Chem. 17 2010 1382 1393
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1382-1393
    • Howlett, A.C.1    Blume, L.C.2    Dalton, G.D.3
  • 2
    • 48249097797 scopus 로고    scopus 로고
    • Endocannabinoids: Synthesis and degradation
    • V. Di Marzo Endocannabinoids: synthesis and degradation Rev. Physiol. Biochem. Pharmacol. 160 2008 1 24
    • (2008) Rev. Physiol. Biochem. Pharmacol. , vol.160 , pp. 1-24
    • Di Marzo, V.1
  • 3
    • 77950660113 scopus 로고    scopus 로고
    • Endocannabinoids as regulators of transient receptor potential (TRP) channels: A further opportunity to develop new endocannabinoid-based therapeutic drugs
    • V. Di Marzo, and L. De Petrocellis Endocannabinoids as regulators of transient receptor potential (TRP) channels: a further opportunity to develop new endocannabinoid-based therapeutic drugs Curr. Med. Chem. 17 2010 1430 1449
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1430-1449
    • Di Marzo, V.1    De Petrocellis, L.2
  • 4
    • 77950634824 scopus 로고    scopus 로고
    • From surface to nuclear receptors: The endocannabinoid family extends its assets
    • M. Pistis, and M. Melis From surface to nuclear receptors: the endocannabinoid family extends its assets Curr. Med. Chem. 17 2010 1450 1467
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1450-1467
    • Pistis, M.1    Melis, M.2
  • 5
    • 0035060264 scopus 로고    scopus 로고
    • Anticonvulsant activity of N-palmitoylethanolamide, a putative endocannabinoid, in mice
    • D.M. Lambert, S. Vandevoorde, G. Diependaele, S.J. Govaerts, and A.R. Robert Anticonvulsant activity of N-palmitoylethanolamide, a putative endocannabinoid, in mice Epilepsia 42 2001 321 327
    • (2001) Epilepsia , vol.42 , pp. 321-327
    • Lambert, D.M.1    Vandevoorde, S.2    Diependaele, G.3    Govaerts, S.J.4    Robert, A.R.5
  • 6
    • 77956648769 scopus 로고    scopus 로고
    • Analysis of gene expression pattern reveals potential targets of dietary oleoylethanolamide in reducing body fat gain in C3H mice
    • C. Thabuis, F. Destaillats, J.F. Landrier, D. Tissot-Favre, and J.C. Martin Analysis of gene expression pattern reveals potential targets of dietary oleoylethanolamide in reducing body fat gain in C3H mice Nutr. Biochem. 21 2010 922 928
    • (2010) Nutr. Biochem. , vol.21 , pp. 922-928
    • Thabuis, C.1    Destaillats, F.2    Landrier, J.F.3    Tissot-Favre, D.4    Martin, J.C.5
  • 7
    • 0037103724 scopus 로고    scopus 로고
    • Binding, degradation and apoptotic activity of stearoylethanolamide in rat C6 glioma cells
    • M. Maccarrone, R. Pauselli, M. Di Rienzo, and A. Finazzi-Agrò Binding, degradation and apoptotic activity of stearoylethanolamide in rat C6 glioma cells Biochem. J. 366 2002 137 144
    • (2002) Biochem. J. , vol.366 , pp. 137-144
    • MacCarrone, M.1    Pauselli, R.2    Di Rienzo, M.3    Finazzi-Agrò, A.4
  • 8
    • 33646521012 scopus 로고    scopus 로고
    • Diurnal variation of arachidonoylethanolamine, palmitoylethanolamide and oleoylethanolamide in the brain of the rat
    • E. Murillo-Rodriguez, F. Desarnaud, and O. Prospero-Garcia Diurnal variation of arachidonoylethanolamine, palmitoylethanolamide and oleoylethanolamide in the brain of the rat Life Sci. 79 2006 30 37
    • (2006) Life Sci. , vol.79 , pp. 30-37
    • Murillo-Rodriguez, E.1    Desarnaud, F.2    Prospero-Garcia, O.3
  • 9
    • 0242268553 scopus 로고    scopus 로고
    • The molecular logic of endocannabinoid signalling
    • D. Piomelli The molecular logic of endocannabinoid signalling Nat. Rev. Neurosci. 4 2003 873 884
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 873-884
    • Piomelli, D.1
  • 10
    • 78049232267 scopus 로고    scopus 로고
    • Intracellular trafficking of anandamide: New concepts for signaling
    • M. Maccarrone, E. Dainese, and S. Oddi Intracellular trafficking of anandamide: new concepts for signaling Trends Biochem. Sci. 35 2010 601 608
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 601-608
    • MacCarrone, M.1    Dainese, E.2    Oddi, S.3
  • 11
    • 51349141952 scopus 로고    scopus 로고
    • Endocannabinoid signaling as a synaptic circuit breaker in neurological disease
    • I. Katona, and T.F. Freund Endocannabinoid signaling as a synaptic circuit breaker in neurological disease Nat. Med. 14 2008 923 930
    • (2008) Nat. Med. , vol.14 , pp. 923-930
    • Katona, I.1    Freund, T.F.2
  • 12
    • 42449097191 scopus 로고    scopus 로고
    • Endocannabinoids, adipose tissue and lipid metabolism
    • C. Pagano, M. Rossato, and R. Vettor Endocannabinoids, adipose tissue and lipid metabolism J. Neuroendocrinol. 1 2008 124 129
    • (2008) J. Neuroendocrinol. , vol.1 , pp. 124-129
    • Pagano, C.1    Rossato, M.2    Vettor, R.3
  • 13
    • 70350072546 scopus 로고    scopus 로고
    • Endocannabinoids: Friends and foes of reproduction
    • M. Maccarrone Endocannabinoids: friends and foes of reproduction Prog. Lipid Res. 48 2009 344 354
    • (2009) Prog. Lipid Res. , vol.48 , pp. 344-354
    • MacCarrone, M.1
  • 14
    • 67749086243 scopus 로고    scopus 로고
    • The emerging role of the endocannabinoid system in cardiovascular disease
    • P. Pacher, and S. Steffens The emerging role of the endocannabinoid system in cardiovascular disease Semin. Immunopathol. 31 2009 63 77
    • (2009) Semin. Immunopathol. , vol.31 , pp. 63-77
    • Pacher, P.1    Steffens, S.2
  • 15
    • 67649865359 scopus 로고    scopus 로고
    • Endocannabinoid chemical biology: A tool for the development of novel therapy
    • S. Petrosino, A. Ligresti, and V. Di Marzo Endocannabinoid chemical biology: a tool for the development of novel therapy Curr. Opin. Chem. Biol. 13 2009 309 320
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 309-320
    • Petrosino, S.1    Ligresti, A.2    Di Marzo, V.3
  • 16
    • 79960691737 scopus 로고    scopus 로고
    • The highs and lows of cannabinoid receptor expression in disease: Mechanisms and their therapeutic implications
    • L.K. Miller, and L.A. Devi The highs and lows of cannabinoid receptor expression in disease: mechanisms and their therapeutic implications Pharmacol. Rev. 63 2011 461 740
    • (2011) Pharmacol. Rev. , vol.63 , pp. 461-740
    • Miller, L.K.1    Devi, L.A.2
  • 18
    • 78751514576 scopus 로고    scopus 로고
    • An anatomical and temporal portrait of physiological substrates for fatty acid amide hydrolase
    • J.Z. Long, M. La Cava, X. Jin, and B.F. Cravatt An anatomical and temporal portrait of physiological substrates for fatty acid amide hydrolase J. Lipid Res. 52 2011 337 344
    • (2011) J. Lipid Res. , vol.52 , pp. 337-344
    • Long, J.Z.1    La Cava, M.2    Jin, X.3    Cravatt, B.F.4
  • 21
    • 79952118933 scopus 로고    scopus 로고
    • Role of endocannabinoid signaling in anxiety and depression
    • S. Patel, and C.J. Hillard Role of endocannabinoid signaling in anxiety and depression Curr. Top. Behav. Neurosci. 1 2009 347 371
    • (2009) Curr. Top. Behav. Neurosci. , vol.1 , pp. 347-371
    • Patel, S.1    Hillard, C.J.2
  • 23
    • 71749089107 scopus 로고    scopus 로고
    • Pain and beyond: Fatty acid amides and fatty acid amide hydrolase inhibitors in cardiovascular and metabolic diseases
    • S. Pillarisetti, C.W. Alexander, and I. Khanna Pain and beyond: fatty acid amides and fatty acid amide hydrolase inhibitors in cardiovascular and metabolic diseases Drug Discov. Today 14 2009 1098 1111
    • (2009) Drug Discov. Today , vol.14 , pp. 1098-1111
    • Pillarisetti, S.1    Alexander, C.W.2    Khanna, I.3
  • 24
    • 33645299083 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase: A potential target for next generation therapeutics
    • M. Maccarrone Fatty acid amide hydrolase: a potential target for next generation therapeutics Curr. Pharm. Des. 12 2006 759 772
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 759-772
    • MacCarrone, M.1
  • 25
    • 34848863139 scopus 로고    scopus 로고
    • Therapeutic potential of endocannabinoid-hydrolysing enzyme inhibitors
    • S.M. Saario, and J.T. Laitinen Therapeutic potential of endocannabinoid-hydrolysing enzyme inhibitors Basic Clin. Pharmacol. Toxicol. 101 2007 287 293
    • (2007) Basic Clin. Pharmacol. Toxicol. , vol.101 , pp. 287-293
    • Saario, S.M.1    Laitinen, J.T.2
  • 26
    • 2242490907 scopus 로고    scopus 로고
    • Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling
    • M.H. Bracey, M.A. Hanson, K.R. Masuda, R.C. Stevens, and B.F. Cravatt Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling Science 298 2002 1793 1796
    • (2002) Science , vol.298 , pp. 1793-1796
    • Bracey, M.H.1    Hanson, M.A.2    Masuda, K.R.3    Stevens, R.C.4    Cravatt, B.F.5
  • 27
    • 22244484464 scopus 로고    scopus 로고
    • Structure and function of fatty acid amide hydrolase
    • M.K. McKinney, and B.F. Cravatt Structure and function of fatty acid amide hydrolase Annu. Rev. Biochem. 74 2005 411 432
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 411-432
    • McKinney, M.K.1    Cravatt, B.F.2
  • 28
    • 58149296562 scopus 로고    scopus 로고
    • Fatty acid amide hydrolase: A gate-keeper of the endocannabinoid system
    • F. Fezza, C. De Simone, D. Amadio, and M. Maccarrone Fatty acid amide hydrolase: a gate-keeper of the endocannabinoid system Subcell. Biochem. 49 2008 101 132
    • (2008) Subcell. Biochem. , vol.49 , pp. 101-132
    • Fezza, F.1    De Simone, C.2    Amadio, D.3    MacCarrone, M.4
  • 31
    • 33947491800 scopus 로고    scopus 로고
    • Closing the gate to the active site: Effect of the inhibitor methoxyarachidonyl fluorophosphonate on the conformation and membrane binding of fatty acid amide hydrolase
    • G. Mei, A. Di Venere, V. Gasperi, E. Nicolai, K.R. Masuda, A. Finazzi-Agrò, B.F. Cravatt, and M. Maccarrone Closing the gate to the active site: effect of the inhibitor methoxyarachidonyl fluorophosphonate on the conformation and membrane binding of fatty acid amide hydrolase J. Biol. Chem. 282 2007 3829 3836
    • (2007) J. Biol. Chem. , vol.282 , pp. 3829-3836
    • Mei, G.1    Di Venere, A.2    Gasperi, V.3    Nicolai, E.4    Masuda, K.R.5    Finazzi-Agrò, A.6    Cravatt, B.F.7    MacCarrone, M.8
  • 32
    • 0032573124 scopus 로고    scopus 로고
    • Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: Identification of the transmembrane domain as a site for oligomerization
    • M.P. Patricelli, H.A. Lashuel, D.K. Giang, J.W. Kelly, and B.F. Cravatt Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization Biochemistry 37 1998 15177 15187
    • (1998) Biochemistry , vol.37 , pp. 15177-15187
    • Patricelli, M.P.1    Lashuel, H.A.2    Giang, D.K.3    Kelly, J.W.4    Cravatt, B.F.5
  • 33
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • J.T. Yang, C.S. Wu, and H.M. Martinez Calculation of protein conformation from circular dichroism Methods Enzymol. 130 1986 208 269
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 35
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • A.G. Szabo, and D.M. Rayner Fluorescence decay of tryptophan conformers in aqueous solution J. Am. Chem. Soc. 102 1980 554 563
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 36
    • 0024991372 scopus 로고
    • Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation
    • N. Rosato, E. Gratton, G. Mei, and A. Finazzi-Agrò Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation Biophys. J. 55 1990 817 822
    • (1990) Biophys. J. , vol.55 , pp. 817-822
    • Rosato, N.1    Gratton, E.2    Mei, G.3    Finazzi-Agrò, A.4
  • 37
    • 77953526759 scopus 로고    scopus 로고
    • A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1
    • E. Dainese, C.B. Angelucci, A. Sabatucci, V. De Filippis, G. Mei, and M. Maccarrone A novel role for iron in modulating the activity and membrane-binding ability of a trimmed soybean lipoxygenase-1 FASEB J. 24 2010 1725 1736
    • (2010) FASEB J. , vol.24 , pp. 1725-1736
    • Dainese, E.1    Angelucci, C.B.2    Sabatucci, A.3    De Filippis, V.4    Mei, G.5    MacCarrone, M.6
  • 38
  • 39
    • 69349085157 scopus 로고    scopus 로고
    • Molecular view of cholesterol flip-flop and chemical potential in different membrane environments
    • W.F. Bennett, J.L. MacCallum, M.J. Hinner, S.J. Marrink, and D.P. Tieleman Molecular view of cholesterol flip-flop and chemical potential in different membrane environments J. Am. Chem. Soc. 131 2009 12714 12720
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12714-12720
    • Bennett, W.F.1    MacCallum, J.L.2    Hinner, M.J.3    Marrink, S.J.4    Tieleman, D.P.5
  • 40
    • 15744385109 scopus 로고    scopus 로고
    • Characterization of the fatty acid amide hydrolase inhibitor cyclohexyl carbamic acid 3'-carbamoyl-biphenyl-3-yl ester (URB597): Effects on anandamide and oleoylethanolamide deactivation
    • D. Fegley, S. Gaetani, A. Duranti, A. Tontini, M. Mor, G. Tarzia, and D. Piomelli Characterization of the fatty acid amide hydrolase inhibitor cyclohexyl carbamic acid 3'-carbamoyl-biphenyl-3-yl ester (URB597): effects on anandamide and oleoylethanolamide deactivation J. Pharmacol. Exp. Ther. 313 2005 352 358
    • (2005) J. Pharmacol. Exp. Ther. , vol.313 , pp. 352-358
    • Fegley, D.1    Gaetani, S.2    Duranti, A.3    Tontini, A.4    Mor, M.5    Tarzia, G.6    Piomelli, D.7
  • 42
    • 4744354729 scopus 로고    scopus 로고
    • Cyclohexylcarbamic acid 3'- or 4'-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: Synthesis, quantitative structure-activity relationships, and molecular modeling studies
    • M. Mor, S. Rivara, A. Lodola, P.V. Plazzi, G. Tarzia, A. Duranti, A. Tontini, G. Piersanti, S. Kathuria, and D. Piomelli Cyclohexylcarbamic acid 3'- or 4'-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: synthesis, quantitative structure-activity relationships, and molecular modeling studies J. Med. Chem. 47 2004 4998 5008
    • (2004) J. Med. Chem. , vol.47 , pp. 4998-5008
    • Mor, M.1    Rivara, S.2    Lodola, A.3    Plazzi, P.V.4    Tarzia, G.5    Duranti, A.6    Tontini, A.7    Piersanti, G.8    Kathuria, S.9    Piomelli, D.10
  • 47
    • 0027501381 scopus 로고
    • Circular dichroic analysis of denatured proteins: Inclusion of denatured proteins in the reference set
    • S.Y. Venyaminov, I.A. Baikalov, Z.M. Shen, C.S. Wu, and J.T. Yang Circular dichroic analysis of denatured proteins: inclusion of denatured proteins in the reference set Anal. Biochem. 214 1993 17 24
    • (1993) Anal. Biochem. , vol.214 , pp. 17-24
    • Venyaminov, S.Y.1    Baikalov, I.A.2    Shen, Z.M.3    Wu, C.S.4    Yang, J.T.5
  • 48
    • 50849087043 scopus 로고    scopus 로고
    • Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability
    • G. Mei, A. Di Venere, E. Nicolai, C.B. Angelucci, I. Ivanov, A. Sabatucci, E. Dainese, H. Kuhn, and M. Maccarrone Structural properties of plant and mammalian lipoxygenases. Temperature-dependent conformational alterations and membrane binding ability Biochemistry 47 2008 9234 9242
    • (2008) Biochemistry , vol.47 , pp. 9234-9242
    • Mei, G.1    Di Venere, A.2    Nicolai, E.3    Angelucci, C.B.4    Ivanov, I.5    Sabatucci, A.6    Dainese, E.7    Kuhn, H.8    MacCarrone, M.9
  • 50
    • 0026018961 scopus 로고
    • Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellar phosphatidylcholine dispersions
    • B.J. Litman, E.N. Lewis, and I.W. Levin Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellar phosphatidylcholine dispersions Biochemistry 30 1991 313 319
    • (1991) Biochemistry , vol.30 , pp. 313-319
    • Litman, B.J.1    Lewis, E.N.2    Levin, I.W.3
  • 51
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • L.J. Pike Lipid rafts: bringing order to chaos J. Lipid Res. 44 2003 655 667
    • (2003) J. Lipid Res. , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 52
    • 35748964430 scopus 로고    scopus 로고
    • Modulation of the endocannabinoid system by lipid rafts
    • E. Dainese, S. Oddi, M. Bari, and M. Maccarrone Modulation of the endocannabinoid system by lipid rafts Curr. Med. Chem. 14 2007 2702 2715
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2702-2715
    • Dainese, E.1    Oddi, S.2    Bari, M.3    MacCarrone, M.4
  • 53
    • 74549185125 scopus 로고    scopus 로고
    • FAAH and MAGL inhibitors: Therapeutic opportunities from regulating endocannabinoid levels
    • S. Petrosino, and V. Di Marzo FAAH and MAGL inhibitors: therapeutic opportunities from regulating endocannabinoid levels Curr. Opin. Investig. Drugs 11 2010 51 62
    • (2010) Curr. Opin. Investig. Drugs , vol.11 , pp. 51-62
    • Petrosino, S.1    Di Marzo, V.2
  • 54
    • 80052788690 scopus 로고    scopus 로고
    • Application of computational methods to the design of fatty acid amide hydrolase (FAAH) inhibitors based on a carbamic template structure
    • A. Lodola, S. Rivara, and M. Mor Application of computational methods to the design of fatty acid amide hydrolase (FAAH) inhibitors based on a carbamic template structure Adv. Protein Chem. Struct. Biol. 85 2011 1 26
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.85 , pp. 1-26
    • Lodola, A.1    Rivara, S.2    Mor, M.3
  • 55
    • 79960901769 scopus 로고    scopus 로고
    • The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH)
    • K. Otrubova, C. Ezzili, and D.L. Boger The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH) Bioorg. Med. Chem. Lett. 21 2011 4674 4685
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 4674-4685
    • Otrubova, K.1    Ezzili, C.2    Boger, D.L.3
  • 57
    • 0038381477 scopus 로고    scopus 로고
    • Structure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity
    • A. Di Venere, M.L. Salucci, G. van Zadelhoff, G. Veldink, G. Mei, N. Rosato, A. Finazzi-Agrò, and M. Maccarrone Structure-to-function relationship of mini-lipoxygenase, a 60-kDa fragment of soybean lipoxygenase-1 with lower stability but higher enzymatic activity J. Biol. Chem. 278 2003 18281 18288
    • (2003) J. Biol. Chem. , vol.278 , pp. 18281-18288
    • Di Venere, A.1    Salucci, M.L.2    Van Zadelhoff, G.3    Veldink, G.4    Mei, G.5    Rosato, N.6    Finazzi-Agrò, A.7    MacCarrone, M.8
  • 61
    • 79955383220 scopus 로고    scopus 로고
    • Reversible competitive α-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: Orally active, long-acting analgesics
    • C. Ezzili, M. Mileni, N. McGlinchey, J.Z. Long, S.G. Kinsey, D.G. Hochstatter, R.C. Stevens, A.H. Lichtman, B.F. Cravatt, E.J. Bilsky, and D.L. Boger Reversible competitive α-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: orally active, long-acting analgesics J. Med. Chem. 54 2011 2805 2822
    • (2011) J. Med. Chem. , vol.54 , pp. 2805-2822
    • Ezzili, C.1    Mileni, M.2    McGlinchey, N.3    Long, J.Z.4    Kinsey, S.G.5    Hochstatter, D.G.6    Stevens, R.C.7    Lichtman, A.H.8    Cravatt, B.F.9    Bilsky, E.J.10    Boger, D.L.11
  • 63
    • 77950632004 scopus 로고    scopus 로고
    • Interaction of endocannabinoid receptors with biological membranes
    • E. Dainese, S. Oddi, and M. Maccarrone Interaction of endocannabinoid receptors with biological membranes Curr. Med. Chem. 17 2010 1487 1499
    • (2010) Curr. Med. Chem. , vol.17 , pp. 1487-1499
    • Dainese, E.1    Oddi, S.2    MacCarrone, M.3
  • 64
    • 33845981826 scopus 로고    scopus 로고
    • A second fatty acid amide hydrolase with variable distribution among placental mammals
    • B.Q. Wei, T.S. Mikkelsen, M.K. McKinney, E.S. Lander, and B.F. Cravatt A second fatty acid amide hydrolase with variable distribution among placental mammals J. Biol. Chem. 281 2006 36569 36578
    • (2006) J. Biol. Chem. , vol.281 , pp. 36569-36578
    • Wei, B.Q.1    Mikkelsen, T.S.2    McKinney, M.K.3    Lander, E.S.4    Cravatt, B.F.5
  • 65
    • 79960290509 scopus 로고    scopus 로고
    • Cannabinoid receptor signalling in neurodegenerative diseases: A potential role for membrane fluidity disturbance
    • M. Maccarrone, G. Bernardi, A. Finazzi-Agrò, and D. Centonze Cannabinoid receptor signalling in neurodegenerative diseases: a potential role for membrane fluidity disturbance Br. J. Pharmacol. 163 2011 1379 1390
    • (2011) Br. J. Pharmacol. , vol.163 , pp. 1379-1390
    • MacCarrone, M.1    Bernardi, G.2    Finazzi-Agrò, A.3    Centonze, D.4


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